LMOD2_RAT
ID LMOD2_RAT Reviewed; 549 AA.
AC A1A5Q0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Leiomodin-2;
DE AltName: Full=Cardiac leiomodin;
DE Short=C-LMOD;
DE AltName: Full=Leiomodin {ECO:0000303|PubMed:18403713};
GN Name=Lmod2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18403713; DOI=10.1126/science.1155313;
RA Chereau D., Boczkowska M., Skwarek-Maruszewska A., Fujiwara I., Hayes D.B.,
RA Rebowski G., Lappalainen P., Pollard T.D., Dominguez R.;
RT "Leiomodin is an actin filament nucleator in muscle cells.";
RL Science 320:239-243(2008).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=20685966; DOI=10.1091/mbc.e10-02-0109;
RA Skwarek-Maruszewska A., Boczkowska M., Zajac A.L., Kremneva E.,
RA Svitkina T., Dominguez R., Lappalainen P.;
RT "Different localizations and cellular behaviors of leiomodin and
RT tropomodulin in mature cardiomyocyte sarcomeres.";
RL Mol. Biol. Cell 21:3352-3361(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15; SER-24 AND
RP SER-406, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Mediates nucleation of actin filaments and thereby promotes
CC actin polymerization (PubMed:18403713). Plays a role in the regulation
CC of actin filament length (By similarity). Required for normal sarcomere
CC organization in the heart, and for normal heart function
CC (PubMed:18403713). {ECO:0000250|UniProtKB:Q6P5Q4,
CC ECO:0000269|PubMed:18403713}.
CC -!- SUBUNIT: Can bind at least three actin monomers and thereby provides a
CC nucleus for actin filament formation. Interacts (via N-terminus) with
CC tropomyosin alpha (TPM1) (via N-terminus). May also interact with TPM2
CC (via N-terminus). {ECO:0000250|UniProtKB:Q6P5Q4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:20685966}. Cytoplasm,
CC myofibril {ECO:0000269|PubMed:20685966}. Cytoplasm, myofibril,
CC sarcomere, M line {ECO:0000269|PubMed:18403713}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:18403713}. Note=Colocalizes with actin
CC filaments in sarcomeres. Detected close to the M line.
CC {ECO:0000269|PubMed:18403713}.
CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR EMBL; BC128755; AAI28756.1; -; mRNA.
DR RefSeq; NP_001094434.1; NM_001100964.1.
DR AlphaFoldDB; A1A5Q0; -.
DR SMR; A1A5Q0; -.
DR STRING; 10116.ENSRNOP00000067847; -.
DR iPTMnet; A1A5Q0; -.
DR PhosphoSitePlus; A1A5Q0; -.
DR jPOST; A1A5Q0; -.
DR PaxDb; A1A5Q0; -.
DR PeptideAtlas; A1A5Q0; -.
DR PRIDE; A1A5Q0; -.
DR GeneID; 296935; -.
DR KEGG; rno:296935; -.
DR CTD; 442721; -.
DR RGD; 1592092; Lmod2.
DR eggNOG; KOG3735; Eukaryota.
DR InParanoid; A1A5Q0; -.
DR OrthoDB; 1025132at2759; -.
DR PhylomeDB; A1A5Q0; -.
DR PRO; PR:A1A5Q0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0097512; C:cardiac myofibril; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0030017; C:sarcomere; IDA:UniProtKB.
DR GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR GO; GO:0005523; F:tropomyosin binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; ISO:RGD.
DR GO; GO:0045010; P:actin nucleation; ISS:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR GO; GO:0051694; P:pointed-end actin filament capping; IEA:InterPro.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR030132; LMOD2.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR004934; TMOD.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR PANTHER; PTHR10901:SF12; PTHR10901:SF12; 1.
DR Pfam; PF03250; Tropomodulin; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..549
FT /note="Leiomodin-2"
FT /id="PRO_0000311342"
FT DOMAIN 523..542
FT /note="WH2"
FT REGION 1..164
FT /note="Interaction with actin 1"
FT /evidence="ECO:0000250|UniProtKB:Q6P5Q4"
FT REGION 1..47
FT /note="Interaction with tropomyosin alpha"
FT /evidence="ECO:0000250|UniProtKB:Q6P5Q4"
FT REGION 1..42
FT /note="Tropomyosin-binding"
FT /evidence="ECO:0000250"
FT REGION 91..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..499
FT /note="Interaction with actin 2"
FT /evidence="ECO:0000250|UniProtKB:Q6P5Q4"
FT REGION 179..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..542
FT /note="Interaction with actin 3"
FT /evidence="ECO:0000250|UniProtKB:Q6P5Q4"
FT COILED 457..515
FT /evidence="ECO:0000255"
FT COMPBIAS 95..141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..453
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 549 AA; 61717 MW; 3494F88AEA5C395C CRC64;
MSTFGYRRGL SKYESIDEDE LLASLTAEEL KELERELEDI EPDRNLPVGL RQKSLTEKTP
TGNFSREALM AYWEKESQKL LEKERLGECG KLAEEDKEES EEELIFTESN SEVSEEVCTE
EEEESTEEEE EEEEEDSEEE EVTTEVTKHI NGTVSHNGVN PDNSKPKTFK SQIENINLTN
GNSGGTQRNT ESPAAIHPCG NPTVIEDALE KIKNNDPDTT EVNLNNIENI TTQTLSRFAE
ALKENTVVKT FSLANTHADD AAAIAIAEML KVNEHITSVN VESNFITGKG ILAIMRALQH
NTVLTELRFH NQRHIMGSQV EMEIVKLLKE NTTLLRLGYH FELPGPRMSM TSILTRNMDK
QRQKRMQEQK QQEGHDGGAT LRTKVWQRGT PGSSPYASPR QSPWSSPKVS KKVHTGRSRP
PSPVAPPPPP PPPPLPPHML PPPPPPPAPP LPGKKLITRN IAEVIKQQES AQRALQNGQR
KKKGKKVKKQ PNNILKEIKN SLRSVQEKKM EESSRPSTPQ RSAHENLMEA IRGSSIRQLR
RVEVPEALR
